메뉴 건너뛰기




Volumn 111, Issue 1-2, 2006, Pages 219-227

Silk fibroin as an organic polymer for controlled drug delivery

Author keywords

Biomaterials; Drug delivery; FTIR; Silk fibroin; Wide angle X ray scattering

Indexed keywords

CRYSTALLINE MATERIALS; DRUG PRODUCTS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MOLECULAR WEIGHT; PROTEINS; X RAY SCATTERING;

EID: 33344470196     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2005.12.009     Document Type: Article
Times cited : (340)

References (51)
  • 2
    • 2242434437 scopus 로고    scopus 로고
    • Conformation transition in silk protein films monitored by time-resolved Fourier transform infrared spectroscopy: Effect of potassium ions on Nephila spidroin films
    • X. Chen, D.P. Knight, Z. Shao, and F. Vollrath Conformation transition in silk protein films monitored by time-resolved Fourier transform infrared spectroscopy: effect of potassium ions on Nephila spidroin films Biochemistry 41 50 2002 14944 14950
    • (2002) Biochemistry , vol.41 , Issue.50 , pp. 14944-14950
    • Chen, X.1    Knight, D.P.2    Shao, Z.3    Vollrath, F.4
  • 3
    • 0036678028 scopus 로고    scopus 로고
    • The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
    • J.D. van Beek, S. Hess, F. Vollrath, and B.H. Meier The molecular structure of spider dragline silk: folding and orientation of the protein backbone Proc. Natl. Acad. Sci. U. S. A. 99 16 2002 10266 10271
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.16 , pp. 10266-10271
    • Van Beek, J.D.1    Hess, S.2    Vollrath, F.3    Meier, B.H.4
  • 4
    • 0035935694 scopus 로고    scopus 로고
    • The effect of spinning conditions on the mechanics of a spider's dragline silk
    • F. Vollrath, B. Madsen, and Z. Shao The effect of spinning conditions on the mechanics of a spider's dragline silk Proc. R. Soc. Lond., B Biol. Sci. 268 1483 2001 2339 2346
    • (2001) Proc. R. Soc. Lond., B Biol. Sci. , vol.268 , Issue.1483 , pp. 2339-2346
    • Vollrath, F.1    Madsen, B.2    Shao, Z.3
  • 5
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • D. Wilson, R. Valluzzi, and D. Kaplan Conformational transitions in model silk peptides Biophys. J. 78 5 2000 2690 2701
    • (2000) Biophys. J. , vol.78 , Issue.5 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 7
    • 0035967162 scopus 로고    scopus 로고
    • Liquid crystalline spinning of spider silk
    • F. Vollrath, and D.P. Knight Liquid crystalline spinning of spider silk Nature 410 6828 2001 541 548
    • (2001) Nature , vol.410 , Issue.6828 , pp. 541-548
    • Vollrath, F.1    Knight, D.P.2
  • 10
    • 0034252735 scopus 로고    scopus 로고
    • Lessons from nature-protein fibers
    • K.H. Guhrs, K. Weisshart, and F. Grosse Lessons from nature-protein fibers J. Biotechnol. 74 2 2000 121 134
    • (2000) J. Biotechnol. , vol.74 , Issue.2 , pp. 121-134
    • Guhrs, K.H.1    Weisshart, K.2    Grosse, F.3
  • 11
    • 0037102416 scopus 로고    scopus 로고
    • Surprising strength of silkworm silk
    • Z. Shao, and F. Vollrath Surprising strength of silkworm silk Nature 418 6899 2002 741
    • (2002) Nature , vol.418 , Issue.6899 , pp. 741
    • Shao, Z.1    Vollrath, F.2
  • 12
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • H.J. Jin, and D.L. Kaplan Mechanism of silk processing in insects and spiders Nature 424 6952 2003 1057 1061
    • (2003) Nature , vol.424 , Issue.6952 , pp. 1057-1061
    • Jin, H.J.1    Kaplan, D.L.2
  • 18
    • 16344365086 scopus 로고    scopus 로고
    • Development of an ELISA for quantifying lysozyme in hen egg white
    • M.L. Vidal, J. Gautron, and Y. Nys Development of an ELISA for quantifying lysozyme in hen egg white J. Agric. Food Chem. 53 7 2005 2379 2385
    • (2005) J. Agric. Food Chem. , vol.53 , Issue.7 , pp. 2379-2385
    • Vidal, M.L.1    Gautron, J.2    Nys, Y.3
  • 19
    • 0032485605 scopus 로고    scopus 로고
    • Morphology and crystal structure of a recombinant silk-like molecule, SLP4
    • J.P. Anderson Morphology and crystal structure of a recombinant silk-like molecule, SLP4 Biopolymers 45 1998 307 321
    • (1998) Biopolymers , vol.45 , pp. 307-321
    • Anderson, J.P.1
  • 20
    • 0035895432 scopus 로고    scopus 로고
    • A repeated beta-turn structure in poly(Ala-Gly) as a model for silk I of Bombyx mori silk fibroin studied with two dimensional spin-diffusion NMS under off magic angle spinning and rotational echo double resistance
    • T. Asakura, J. Ashida, T. Yamane, T. Kameda, Y. Nakazawa, K. Ohgo, and K. Komatsu A repeated beta-turn structure in poly(Ala-Gly) as a model for silk I of Bombyx mori silk fibroin studied with two dimensional spin-diffusion NMS under off magic angle spinning and rotational echo double resistance J. Mol. Biol. 306 2 2001 291 305
    • (2001) J. Mol. Biol. , vol.306 , Issue.2 , pp. 291-305
    • Asakura, T.1    Ashida, J.2    Yamane, T.3    Kameda, T.4    Nakazawa, Y.5    Ohgo, K.6    Komatsu, K.7
  • 21
    • 0031080850 scopus 로고    scopus 로고
    • NMR study of silk I structure of Bombyx mori silk fibroin with N-15- and C-13-NMR chemical shift contour plots
    • T. Asakura, M. Demura, T. Date, N. Miyashita, K. Ogawa, and M.P. Williamson NMR study of silk I structure of Bombyx mori silk fibroin with N-15- and C-13-NMR chemical shift contour plots Biopolymers 41 1997 193 203
    • (1997) Biopolymers , vol.41 , pp. 193-203
    • Asakura, T.1    Demura, M.2    Date, T.3    Miyashita, N.4    Ogawa, K.5    Williamson, M.P.6
  • 22
    • 0035045539 scopus 로고    scopus 로고
    • Structure of Bombyx mori silk fibroin before spinning in solid state studied with wide angle X-ray scattering and (13)C cross-polarization/magic angle spinning NMR
    • T. Asakura, T. Yamane, Y. Nakazawa, T. Kameda, and K. Ando Structure of Bombyx mori silk fibroin before spinning in solid state studied with wide angle X-ray scattering and (13)C cross-polarization/magic angle spinning NMR Biopolymers 58 5 2001 521 525
    • (2001) Biopolymers , vol.58 , Issue.5 , pp. 521-525
    • Asakura, T.1    Yamane, T.2    Nakazawa, Y.3    Kameda, T.4    Ando, K.5
  • 23
    • 0026253604 scopus 로고
    • Conformational energy studies of beta-sheets of model silk fibroin peptides: I. Sheets of poly(Ala-Gly) chains
    • S.A. Fossey, G. Nemethy, K.D. Gibson, and H.A. Scheraga Conformational energy studies of beta-sheets of model silk fibroin peptides: I. Sheets of poly(Ala-Gly) chains Biopolymers 31 13 1991 1529 1541
    • (1991) Biopolymers , vol.31 , Issue.13 , pp. 1529-1541
    • Fossey, S.A.1    Nemethy, G.2    Gibson, K.D.3    Scheraga, H.A.4
  • 25
    • 0005169077 scopus 로고
    • An unstable lattice in silk fibroin
    • O. Kratky, E. Schauenstein, and A. Sekora An unstable lattice in silk fibroin Nature 165 1950 319 320
    • (1950) Nature , vol.165 , pp. 319-320
    • Kratky, O.1    Schauenstein, E.2    Sekora, A.3
  • 26
    • 0015223463 scopus 로고
    • Crystal structure of poly(l-Ala-Gly)II. a model for silk. I
    • B. Lotz, and H.D. Keith Crystal structure of poly(l-Ala-Gly)II. A model for silk. I J. Mol. Biol. 61 1 1971 201 215
    • (1971) J. Mol. Biol. , vol.61 , Issue.1 , pp. 201-215
    • Lotz, B.1    Keith, H.D.2
  • 27
    • 85043728630 scopus 로고    scopus 로고
    • Raman spectroscopic characterization of Bombyx mori silk fibroin: Raman spectrum of silk I
    • P. Monti, P. Taddei, G. Freddi, T. Asakura, and M. Tsukada Raman spectroscopic characterization of Bombyx mori silk fibroin: raman spectrum of silk I J. Raman Spectrosc. 32 2001 103 107
    • (2001) J. Raman Spectrosc. , vol.32 , pp. 103-107
    • Monti, P.1    Taddei, P.2    Freddi, G.3    Asakura, T.4    Tsukada, M.5
  • 28
    • 0035888273 scopus 로고    scopus 로고
    • Refined molecular and crystal structure of silk I based on Ala-Gly and (Ala-Gly)(2)-Ser-Gly peptide sequence
    • K. Okuyama, R. Somashekar, K. Noguchi, and S. Ichimura Refined molecular and crystal structure of silk I based on Ala-Gly and (Ala-Gly)(2)-Ser-Gly peptide sequence Biopolymers 59 2001 310 319
    • (2001) Biopolymers , vol.59 , pp. 310-319
    • Okuyama, K.1    Somashekar, R.2    Noguchi, K.3    Ichimura, S.4
  • 29
    • 0000890258 scopus 로고
    • High-resolution C-13 NMR-study of silk fibroin in the solid state by the cross-polarization magic ange spinning method-conformational characterization of silk-I and silk-II type forms of Bombyx-mori fibroin by the conformation-dependent C-13 chemical shifts
    • H. Saito, Y. Iwanga, R. Tabeta, M. Narita, and T. Asakura High-resolution C-13 NMR-study of silk fibroin in the solid state by the cross-polarization magic ange spinning method-conformational characterization of silk-I and silk-II type forms of Bombyx-mori fibroin by the conformation-dependent C-13 chemical shifts Macromolecules 17 1984 1405 1412
    • (1984) Macromolecules , vol.17 , pp. 1405-1412
    • Saito, H.1    Iwanga, Y.2    Tabeta, R.3    Narita, M.4    Asakura, T.5
  • 30
    • 0141459939 scopus 로고    scopus 로고
    • Molecular dynamics simulation of conformational change of poly(Ala-Gly) from silk I to silk II in relation to fiber formation mechanism of Bombyx mori silk fibroin
    • T. Yamane, K. Umemura, Y. Nakazawa, and T. Asakura Molecular dynamics simulation of conformational change of poly(Ala-Gly) from silk I to silk II in relation to fiber formation mechanism of Bombyx mori silk fibroin Macromolecules 36 2003 6766 6772
    • (2003) Macromolecules , vol.36 , pp. 6766-6772
    • Yamane, T.1    Umemura, K.2    Nakazawa, Y.3    Asakura, T.4
  • 31
    • 0000951118 scopus 로고
    • Conformation characterization of Bombyx mori silk fibroin in the solid-state by high-frequency C-13 cross-polarization magic angle spinning NMR, X-Ray Diffraction, and Infrared Spectroscopy
    • T. Asakura, A. Kuzuhara, R. Tabeta, and H. Saito Conformation characterization of Bombyx mori silk fibroin in the solid-state by high-frequency C-13 cross-polarization magic angle spinning NMR, X-Ray Diffraction, and Infrared Spectroscopy Macromolecules 18 1985 1841 1845
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 32
    • 38349006853 scopus 로고
    • An investigation of the structure of silk fibroin
    • R.E. Marsh, R.B. Corey, and L. Pauling An investigation of the structure of silk fibroin Biochim. Biophys. Acta 16 1 1955 1 34
    • (1955) Biochim. Biophys. Acta , vol.16 , Issue.1 , pp. 1-34
    • Marsh, R.E.1    Corey, R.B.2    Pauling, L.3
  • 36
    • 0033527151 scopus 로고    scopus 로고
    • In vitro evaluation of the inflammatory potential of the silk fibroin
    • M. Santin, A. Motta, G. Freddi, and M. Cannas In vitro evaluation of the inflammatory potential of the silk fibroin J. Biomed. Mater. Res. 46 3 1999 382 389
    • (1999) J. Biomed. Mater. Res. , vol.46 , Issue.3 , pp. 382-389
    • Santin, M.1    Motta, A.2    Freddi, G.3    Cannas, M.4
  • 38
    • 0026526148 scopus 로고
    • Characterization of low-temperature-plasma treated silk fibroin fabrics by ESCA and the use of the fabrics as an enzyme-immobilization support
    • M. Demura, T. Takekawa, T. Asakura, and A. Nishikawa Characterization of low-temperature-plasma treated silk fibroin fabrics by ESCA and the use of the fabrics as an enzyme-immobilization support Biomaterials 13 5 1992 276 280
    • (1992) Biomaterials , vol.13 , Issue.5 , pp. 276-280
    • Demura, M.1    Takekawa, T.2    Asakura, T.3    Nishikawa, A.4
  • 39
    • 0028516254 scopus 로고
    • Preparation and application of porous silk fibroin materials
    • M. Tsukada, G. Freddi, N. Minoura, and G. Allara Preparation and application of porous silk fibroin materials J. Appl. Polym. Sci. 54 1994 507 514
    • (1994) J. Appl. Polym. Sci. , vol.54 , pp. 507-514
    • Tsukada, M.1    Freddi, G.2    Minoura, N.3    Allara, G.4
  • 40
    • 0033120181 scopus 로고    scopus 로고
    • Spectroscopic investigation of tertiary fold of staphylococcal protein a to explore its engineering application
    • J. Kikuchi, Y. Mitsui, T. Asakura, K. Hasuda, H. Araki, and K. Owaku Spectroscopic investigation of tertiary fold of staphylococcal protein A to explore its engineering application Biomaterials 20 7 1999 647 654
    • (1999) Biomaterials , vol.20 , Issue.7 , pp. 647-654
    • Kikuchi, J.1    Mitsui, Y.2    Asakura, T.3    Hasuda, K.4    Araki, H.5    Owaku, K.6
  • 42
    • 0013600471 scopus 로고
    • Protein a with low molecular weight and its immobilization in silk membrane
    • Y. Mitsui, T. Asakura, H. Araki, and K. Hasuda Protein A with low molecular weight and its immobilization in silk membrane Rept. Prog. Polym. Phys. Jpn. 32 1989 613 616
    • (1989) Rept. Prog. Polym. Phys. Jpn. , vol.32 , pp. 613-616
    • Mitsui, Y.1    Asakura, T.2    Araki, H.3    Hasuda, K.4
  • 43
    • 0034829837 scopus 로고    scopus 로고
    • Study on porous silk fibroin materials: I. Fine structure of freeze dried silk fibroin
    • M. Li, S. Lu, Z. Wu, H. Yan, J. Mo, and L. Wang Study on porous silk fibroin materials: I. Fine structure of freeze dried silk fibroin J. Appl. Polym. Sci. 79 12 2001 2185 2191
    • (2001) J. Appl. Polym. Sci. , vol.79 , Issue.12 , pp. 2185-2191
    • Li, M.1    Lu, S.2    Wu, Z.3    Yan, H.4    Mo, J.5    Wang, L.6
  • 44
    • 0015223463 scopus 로고
    • Crystal structure of poly(l-Ala-Gly)II. a model for silk. I.
    • B. Lotz, and H.D. Keith Crystal structure of poly(l-Ala-Gly)II. A model for silk. I. J. Mol. Biol. 61 1 1971 201 215
    • (1971) J. Mol. Biol. , vol.61 , Issue.1 , pp. 201-215
    • Lotz, B.1    Keith, H.D.2
  • 45
    • 0001244437 scopus 로고
    • Solution properties of branched dextrans
    • K.A. Granath Solution properties of branched dextrans J. Colloid Sci. 13 1958 308 328
    • (1958) J. Colloid Sci. , vol.13 , pp. 308-328
    • Granath, K.A.1
  • 47
    • 0345118157 scopus 로고    scopus 로고
    • Mapping domain structures in silks from insects and spiders related to protein assembly
    • E. Bini, D.P. Knight, and D.L. Kaplan Mapping domain structures in silks from insects and spiders related to protein assembly J. Mol. Biol. 335 1 2004 27 40
    • (2004) J. Mol. Biol. , vol.335 , Issue.1 , pp. 27-40
    • Bini, E.1    Knight, D.P.2    Kaplan, D.L.3
  • 51
    • 10044274310 scopus 로고    scopus 로고
    • Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin
    • U.J. Kim, J. Park, H.J. Kim, M. Wada, and D.L. Kaplan Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin Biomaterials 26 15 2005 2775 2785
    • (2005) Biomaterials , vol.26 , Issue.15 , pp. 2775-2785
    • Kim, U.J.1    Park, J.2    Kim, H.J.3    Wada, M.4    Kaplan, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.